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1.

001-es BibID:BIBFORM047427
Első szerző:Adyshev, Djanybek M.
Cím:Ezrin/radixin/moesin proteins differentially regulate endothelial hyperpermeability after thrombin / Djanybek M. Adyshev, Steven M. Dudek, Nurgul Moldobaeva, Kyung-mi Kim, Shwu-Fan Ma, Anita Kasa, Joe G. N. Garcia, Alexander D. Verin
Dátum:2013
ISSN:1040-0605
Megjegyzések:Endothelial cell (EC) barrier disruption induced by inflammatory agonists such as thrombin leads to potentially lethal physiological dysfunction such as alveolar flooding, hypoxemia and pulmonary edema. Thrombin stimulates paracellular gap and F-actin stress fiber formation, triggers actomyosin contraction and alters EC permeability through multiple mechanisms that include protein kinase C (PKC) activation. We previously have shown that the ezrin, radixin, and moesin (ERM) actin-binding proteins differentially participate in S1P-induced EC barrier enhancement. Phosphorylation of a conserved threonine residue in the C terminus of ERM proteins causes conformational changes in ERM to unmask binding sites and is considered a hallmark of ERM activation. In the present study we test the hypothesis that ERM proteins are phosphorylated on this critical threonine residue by thrombin-induced signaling events and explore the role of the ERM family in modulating thrombin-induced cytoskeletal rearrangement and EC barrier function. Thrombin promotes ERM phosphorylation at this threonine residue (Ezrin-567, Radixin-564, Moesin-558) in a PKC-dependent fashion and induces translocation of phosphorylated ERM to the EC periphery. Thrombin-induced ERM threonine phosphorylation is likely synergistically mediated by protease-activated receptors PAR1 and PAR2. Using the siRNA approach, depletion of either moesin alone, or of all three ERM proteins, significantly attenuates thrombin-induced increase in EC barrier permeability (TER), cytoskeletal rearrangements, paracellular gap formation and accumulation of di-phospho-MLC. In contrast, radixin depletion exerts opposing effects on these indices. These data suggest that ERM proteins play important differential roles in the thrombin-induced modulation of EC permeability, with moesin promoting barrier dysfunction and radixin opposing it
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
thrombin
ERM
PKC
phosphorylation
Megjelenés:American Journal of Physiology-Lung Cellular and Molecular Physiology 305 : 3 (2013), p. L240-L255. -
További szerzők:Dudek, Steven Moldobaeva, Nurgul Kim, Kyung-mi Ma, Shwu-Fan Kovács-Kása Anita (1983-) Garcia, Joe G. N. Verin, Alexander
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2.

001-es BibID:BIBFORM058970
Első szerző:Bai Péter (biokémikus)
Cím:Biology of Poly(ADP-Ribose) Polymerases : the Factotums of Cell Maintenance / Peter Bai
Dátum:2015
ISSN:1097-2765
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Molecular Cell. - 58 : 6 (2015), p. 947-958. -
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TÁMOP
OTKA-K108308
OTKA
OTKA-K105872
OTKA
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3.

001-es BibID:BIBFORM028159
Első szerző:Bakó Éva (biokémikus)
Cím:Purification and partial characterization of protein phosphatases from rat thymus / Éva Bakó, Viktor Dombrádi, Ferenc Erdődi, Lawrence Zumo, Pál Kertai, Pál Gergely
Dátum:1989
ISSN:0167-4889
Megjegyzések:Protein phosphatases assayed with phosphorylase alpha are present in the soluble and particulate fractions of rat thymocytes. Phosphorylase phosphatase activity in the cytosol fraction was resolved by heparin-Sepharose chromatography into type-1 and type-2A enzymes. Similarities between thymocyte and muscle or liver protein phosphatase-1 included preferential dephosphorylation of the beta subunit of phosphorylase kinase, inhibition by inhibitor-2 and retention by heparin-Sepharose. Similarities between thymocyte and muscle or liver protein phosphatase-2A included specificity for the alpha subunit of phosphorylase kinase, insensitivity to the action of inhibitor-2, lack of retention by heparin-Sepharose and stimulation by polycationic macromolecules such as polybrene, protamine and histone H1. Protein phosphatase-1 from the cytosol fraction of thymocytes had an apparent molecular mass of 120 kDa as determined by gel filtration. The phosphatase-2A separated from the cytosol of thymocytes may correspond to phosphatase-2A0, since it was completely inactive (latent) in the absence of polycation and had activity only in the presence of polycations. The apparent molecular mass of phosphatase-2A0 from thymocytes was 240 kDa as determined by gel filtration. The catalytic subunit of thymocyte type-1 protein phosphatase was purified with heparin-Sepharose chromatography followed by gel filtration and fast protein liquid chromatography on Mono Q column. The purified type-1 catalytic subunit exhibited a specific activity of 8.2 U/mg and consisted of a single protein of 35 kDa as judged by SDS-gel electrophoresis. The catalytic subunit of type-2A phosphatase from thymocytes appearing in the heparin-Sepharose flow-through fraction was further purified on protamine-Sepharose, followed by gel filtration. The specific activity of the type-2A catalytic subunit was 2.1 U/mg and consisted of a major protein of 34.5 kDa, as revealed by SDS-gel electrophoresis.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
protein phosphatase-1
protein phosphatase-2A
polycation
heparin-Sepharose
thymocyte
rat
egyetemen (Magyarországon) készült közlemény
Megjelenés:Biochimica et Biophysica Acta (BBA). Molecular Cell Research. - 1013 : 3 (1989), p. 300-305. -
További szerzők:Kertai Pál (1927-2016) (népegészségügyi szakember) Dombrádi Viktor (1953-) (biokémikus) Erdődi Ferenc (1953-) (biokémikus) Zumo, Lawrence (1966-) Gergely Pál (1947-) (biokémikus)
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4.

001-es BibID:BIBFORM066467
Első szerző:Boratkó Anita (biokémikus, molekuláris biológus)
Cím:PKC mediated phosphorylation of TIMAP regulates PP1c activity and endothelial barrier function / Anita Boratkó, Csilla Csortos
Dátum:2017
ISSN:0167-4889
Megjegyzések:TGF-β inhibited membrane-associated protein (TIMAP) is greatly expressed in endothelial cell lines and serves as a protein phosphatase 1 (PP1) regulatory subunit. Phosphorylation state of TIMAP, through affecting PP1 activity, has a remarkable effect on endothelial barrier function. Here we present evidence for a previously unidentified PKC phosphorylation site in TIMAP. Protein-protein interaction was detected in pulmonary endothelial cells between endogenous TIMAP and activated PKCα. PKCα phosphorylated the full length recombinant TIMAP in in vitro kinase assay and Ser331 of TIMAP was shown to be phosphorylated by PKC. Phosphorylation of TIMAP upon PKC activation in endothelial cells results in enrichment of TIMAP in the membrane, but no such change can be observed in PKC depleted cells. However, the previously identified PKA/GSK-3β induced enrichment of TIMAP at the plasma membrane was not affected in the absence of PKC. Interaction between TIMAP and the TIMAP-PP1 substrate phospho-ERM was described earlier, but now we show that binding of PKC phosphorylated TIMAP to ERM is severely reduced. This suggests an inhibitory effect of phospho-Ser331 on TIMAP-PP1 activity toward phospho-ERM. Accordingly, phospho-ERM level in the membrane fraction of the phospho-mimic S331D TIMAP mutant transfected cells was increased, but the S331A mutant overexpressing endothelial cells had a lower phospho-ERM level. Consistent with the phospho-ERM level, electric resistance measurements showed that the S331A mutation of TIMAP resulted in faster recovery from the PMA treatment. Taken together, phosphorylation of TIMAP on Ser331 by PKC represents a new mechanism of endothelial barrier regulation, through the inhibition of phospho-ERM dephosphorylation.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochimica et Biophysica Acta (BBA). Molecular Cell Research. - 1864 : 2 (2017), p. 431-439. -
További szerzők:Csortos Csilla (1956-) (biokémikus)
Pályázati támogatás:PD116262(AB)
OTKA
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5.

001-es BibID:BIBFORM074172
Első szerző:Csortos Csilla (biokémikus)
Cím:TIMAP is a positive regulator of pulmonary endothelial barrier function / Csilla Csortos, Istvan Czikora, Natalia V. Bogatcheva, Djanybek M. Adyshev, Christophe Poirier, Gabor Olah, Alexander D. Verin
Dátum:2008
ISSN:1040-0605 1522-1504
Megjegyzések:TGF-?-inhibited membrane-associated protein, TIMAP, is expressed at high levels in endothelial cells (EC). It is regarded as a member of the MYPT (myosin phosphatase target subunit) family of protein phosphatase 1 (PP1) regulatory subunits; however, its function in EC is not clear. In our pull-down experiments, recombinant TIMAP binds preferentially the ?-isoform of the catalytic subunit of PP1 (PP1c?) from pulmonary artery EC. As PP1c?, but not PP1c?, binds with MYPT1 into functional complex, these results suggest that TIMAP is a novel regulatory subunit of myosin phosphatase in EC. TIMAP depletion by small interfering RNA (siRNA) technique attenuates increases in transendothelial electrical resistance induced by EC barrier-protective agents (sphingosine-1-phosphate, ATP) and enhances the effect of barrier-compromising agents (thrombin, nocodazole) demonstrating a barrier-protective role of TIMAP in EC. Immunofluorescent staining revealed colocalization of TIMAP with membrane/cytoskeletal protein, moesin. Moreover, TIMAP coimmunoprecipitates with moesin suggesting the involvement of TIMAP/moesin interaction in TIMAP-mediated EC barrier enhancement. Activation of cAMP/PKA cascade by forskolin, which has a barrier-protective effect against thrombin-induced EC permeability, attenuates thrombin-induced phosphorylation of moesin at the cell periphery of control siRNA-treated EC. On the contrary, in TIMAP-depleted EC, forskolin failed to affect the level of moesin phosphorylation at the cell edges. These results suggest the involvement of TIMAP in PKA-mediated moesin dephosphorylation and the importance of this dephosphorylation in TIMAP-mediated EC barrier protection.protein phosphorylation and dephosphorylation are known to be the key signaling events affecting the status of vascular endothelial barrier (11). Cytoskeletal and intercellular junctional proteins are regulated via reversible phosphorylation of serine (Ser), threonine (Thr), or tyrosine (Tyr) side chains. Based on many recent data, it is apparent that several types of protein phosphatases are intimately involved in the regulation of endothelial barrier function (10, 17, 27?29). However, their regulation is not yet completely understood.Protein phosphatase 1 (PP1) is a multimeric phosphoserine/phosphothreonine-specific phosphatase. One of the four different isoforms, ?, ?, ?1, or ?2, of the catalytic subunit (PP1c) binds to one (or two) protein from a pool of regulatory subunits (R). The holoenzyme forms possess diverse cellular functions. A common structural element of R proteins is a short, conserved PP1c binding motif, (R/K)VXF (3, 9, 10). Different R subunits may direct PP1 holoenzymes to distinct subcellular locations and increase or suppress the activity toward specific substrates (3, 9). Myosin light chain phosphatase (or myosin phosphatase, MP), for example, is composed of PP1c? and two regulatory subunits, namely, a larger targeting/regulatory subunit (myosin phosphatase target subunit, MYPT) and a small regulatory subunit (M20) (2, 10, 14). The activity of MP holoenzyme is increased toward phosphorylated myosin compared with the activity of the PP1c monomer (15).It was recently shown that MP function is not limited to myosin dephosphorylation. The MP regulatory subunit MYPT1 can directly bind to F-actin binding proteins including ERM proteins (ezrin-radixin-moesin family). These proteins could be phosphorylated by either protein kinase C? or Rho kinase (12, 20); phosphorylation renders unfolded ERM protein, enabling its interaction with actin and membrane proteins (20, 21). ERM dephosphorylation by MP seems to affect ERM conformation and cytoskeletal/membrane binding capacities (12, 20). These data indicate that MP not only dephosphorylates myosin, but it is also involved in the regulation of F-actin cytoskeleton.Recently, other proteins of the MYPT family, namely MYPT3, TIMAP (TGF-?-inhibited membrane-associated protein), and myosin binding subunit 85 (MBS85), were identified and characterized from different sources (8, 25, 26). They share some structural features with MYPT1, e.g., all of these proteins contain the PP1c binding motif followed by ankyrin repeats. On the other hand, MYPT3, TIMAP, and MBS85 have their own special features as well. For example, both TIMAP and MYPT3 have COOH-terminal prenylation motif suggesting possible membrane association. The high level of homology with MYPT1 implies that TIMAP, MYPT3, and MBS85 may be regulatory subunits of PP1; however, their physiological significance is not known.TIMAP is a 64-kDa protein expressed at high levels in endothelial cells (EC). As TIMAP mRNA synthesis is strongly downregulated by TGF-?1 (8), it is likely to assume that TIMAP may be an important component of endothelial response to TGF-?1, including apoptosis, capillary morphogenesis, and barrier dysfunction. It is highly homologous to MYPT3 (?45% amino acid homology) and shares its structural features, i.e., PP1c binding motif, ankyrin repeats, prenylation motif, and possible nuclear localization signals (8). Yeast and bacterial two-hybrid screening revealed several potential protein partners for TIMAP (1, 16). For instance, TIMAP interacts with the 37/67-kDa laminin receptor (LAMR1). It was suggested that TIMAP targets PP1c to LAMR1, and LAMR1 is a TIMAP-dependent PP1c substrate (16). Although protein-protein interaction between TIMAP and PP1c was shown by immunoprecipitation, its role in regulating PP1c activity is not clarified yet. In the present work, we present evidence for specific interaction between TIMAP and PP1c?. Furthermore, we show that TIMAP has a barrier-protective role in human pulmonary artery endothelial cells (HPAEC), and we propose that ERM proteins are among its targets.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
transendothelial electrical resistance
small interfering RNA
moesin interaction with protein phosphatase 1
Megjelenés:American Journal Of Physiology-Lung Cellular And Molecular Physiology. - 295 : 3 (2008), p. L440-L450. -
További szerzők:Czikora István (1979-) (vegyész, biokémikus) Bogatcheva, Natalia V. Adyshev, Djanybek M. Poirier, Christophe Oláh Gábor Verin, Alexander
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6.

001-es BibID:BIBFORM047051
035-os BibID:PMID:2157500
Első szerző:Csortos Csilla (biokémikus)
Cím:Phosphorylase phosphatase activities of rat liver in streptozotocin-diabetes / Csilla Csortos, Ilona Farkas, Lloyd Sparks, Tamás Bányász, Tibor Kovács, Pál Gergely
Dátum:1990
ISSN:0167-4889
Megjegyzések:Protein phosphatase-1 and 2A, accounting for all the hepatic activity regulating phosphorylase, were assayed in streptozotocin-induced (8 weeks) diabetic Wistar rats. Cytosolic protein phosphatase-1 and 2A were distinguished by chromatography on heparin-Sepharose and by inhibition with inhibitor-2. Approx. 25-35% increases in type-1 phosphorylase phosphatase activity measured in cytosols were registered in diabetic rats when compared with control and 24 h fasting animals. The enrichment of protein phosphatase-1 in the cytosol of streptozotocin-treated rat livers could not be attributed to the reduced glycogen content with the onset of diabetes, since this elevated level of type-1 phosphatase was not observed in fasting rats with low glycogen content. The translocation of type-1 phosphatase from the particulate fraction into the cytosol was also recorded in trypsin-treated samples of diabetic rat livers. The apparent molecular weight of type-1 phosphatase in the cytosol of control and fasted rats was 160,000 as judged by gel filtration. The type-1 phosphatase activity that was released from the particulate fraction by streptozotocin-induced diabetes identified a further enzyme species (Mr 110,000) in the cytosol. Our data imply that the higher levels of cytosolic protein phosphatase-1 in diabetic rat liver could be a consequence of the dissociation of the catalytic subunit of protein phosphatase-1 and the glycogen-binding subunit in rat livers.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Protein phosphatase
Hepatic metabolism
Diabetes
Fasting
Streptozotocin
Rat liver
Megjelenés:Biochimica et Biophysica Acta (BBA). Molecular Cell Research. - 1052 : 1 (1990), p. 235-241. -
További szerzők:Farkas Ilona (1953-) (biokémikus) Sparks, Lloyd Bányász Tamás (1960-) (élettanász) Kovács Tibor (1929-1994) (élettanász) Gergely Pál (1947-) (biokémikus)
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7.

001-es BibID:BIBFORM001291
Első szerző:Csortos Csilla (biokémikus)
Cím:Regulation of vascular endothelial cell barrier function and cytoskeleton structure by protein phosphatases of the PPP family / Csortos Cs., Kolosova I., Verin A. D.
Dátum:2007
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
endothelial barrier function
Ser/Thr protein phosphatases
Megjelenés:American Journal of Physiology-Lung Cellular and Molecular Phsiology. - 293 (2007), p. L843-L854. -
További szerzők:Kolosova, Irina Verin, Alexander
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8.

001-es BibID:BIBFORM055114
Első szerző:Czifra Gabriella (élettanász)
Cím:Protein kinase Cð promotes proliferation and induces malignant transformation in skeletal muscle / Gabriella Czifra, Attila Szöllősi, Zsuzsanna Nagy, Miklós Boros, István Juhász, Andrea Kiss, Ferenc Erdődi, Tamás Szabó, Ilona Kovács, Miklós Török, László Kovács, Peter M. Blumberg, Tamás Bíró
Dátum:2015
ISSN:1582-1838
Megjegyzések:In this paper, we investigated the isoform-specific roles of certain protein kinase C (PKC) isoforms in the regulation of skeletal muscle growth. Here, we provide the first intriguing functional evidence that nPKCð (originally described as an inhibitor of proliferation in various cells types) is a key player in promoting both in vitro and in vivo skeletal muscle growth. Recombinant overexpression of a constitutively active nPKCð in C2C12 myoblast increased proliferation and inhibited differentiation. Conversely, overexpression of kinase-negative mutant of nPKCð (DN-nPKCð) markedly inhibited cell growth. Moreover, overexpression of nPKCð also stimulated in vivo tumour growth and induced malignant transformation in immunodeficient (SCID) mice whereas that of DN-nPKCð suppressed tumour formation. The role of nPKCð in the formation of rhabdomyosarcoma was also investigated where recombinant overexpression of nPKCð in human rhabdomyosarcoma RD cells also increased cell proliferation and enhanced tumour formation in mouse xenografts. The other isoforms investigated (PKCð, ð,ð) exerted only minor (mostly growth-inhibitory) effects in skeletal muscle cells. Collectively, our data introduce nPKCð as a novel growth-promoting molecule in skeletal muscles and invite further trials to exploit its therapeutic potential in the treatment of skeletal muscle malignancies.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Cellular and Molecular Medicine. - 19 : 2 (2015), p. 396-407. -
További szerzők:Szöllősi Attila Gábor (1982-) (élettanász) Nagy Zsuzsanna (1986-) (élettanász) Boros Miklós Juhász István (1956-) (bőrgyógyász, bőrsebész, kozmetológus, klinikai onkológus) Kiss Andrea (1979-) (biokémikus, vegyész) Erdődi Ferenc (1953-) (biokémikus) Szabó Tamás (1968-) (gyermekgyógyász) Kovács Ilona (1965-) (patológus) Török Miklós (1976-) (pathológus) Kovács László (1939-) (élettanász) Blumberg, Peter M. Bíró Tamás (1968-) (élettanász)
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TÁMOP-4.2.2.A-11/1/KONV-2012-0045
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Molekuláris Orvostudomány Doktori Iskola
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9.

001-es BibID:BIBFORM087277
Első szerző:Douida, Abdennour
Cím:The proteasome activator PA200 regulates expression of genes involved in cell survival upon selective mitochondrial inhibition in neuroblastoma cells / Abdennour Douida, Frank Batista, Agnieszka Robaszkiewicz, Pal Boto, Azzam Aladdin, Mónika Szenykiv, Rita Czinege, László Virág, Krisztina Tar
Dátum:2020
ISSN:1582-1838 1582-4934
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Journal Of Cellular And Molecular Medicine. - 24 : 12 (2020), p. 6716-6730. -
További szerzők:Batista, Frank (1975-) (biokémikus) Robaszkiewicz, Agnieszka (1983-) (biokémikus) Botó Pál (1986-) (molekuláris biológus) Aladdin, Azzam (1980-) (molekuláris biológus) Szenykiv Mónika Czinege Rita Virág László (1965-) (biokémikus, sejtbiológus, farmakológus) Tar Krisztina (1975-) (biokémikus, molekuláris biológus)
Pályázati támogatás:GINOP-2.3.2-15-2016-00020
GINOP
GINOP-2.3.2-15-2016-00048
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OTKA K112336
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OTKA K132193
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10.

001-es BibID:BIBFORM003581
Első szerző:Erdélyi Katalin (molekuláris biológus, biokémikus)
Cím:Pathophysiologic role of oxidative stress-induced poly(ADP-ribose) polymerase-1 activation : focus on cell death and transcriptional regulation / Erdélyi K., Bakondi E., Gergely P., Szabó C., Virág L.
Dátum:2005
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
poly(ADP-ribose) polymerase
cytotoxicity
calcium signal
necrosis
apoptosis
mitochondria
DNA damage
peroxynitrite
Megjelenés:Cellular and Molecular Life Sciences. - 62 : 7-8 (2005), p. 751-759. -
További szerzők:Bakondi Edina (1975-) (biokémikus, vegyész) Gergely Pál (1947-) (biokémikus) Szabó C. Virág László (1965-) (biokémikus, sejtbiológus, farmakológus)
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11.

001-es BibID:BIBFORM028721
Első szerző:Ito, Masaaki
Cím:Myosin phosphatase : structure, regulation and function / Masaaki Ito, Takeshi Nakano, Ferenc Erdődi, David J. Hartshorne
Dátum:2004
ISSN:0300-8177
Megjegyzések:Phosphorylation of myosin II plays an important role in many cell functions, including smooth muscle contraction. The level of myosin II phosphorylation is determined by activities of myosin light chain kinase and myosin phosphatase (MP). MP is composed of 3 subunits: a catalytic subunit of type 1 phosphatase, PPlc; a targeting subunit, termed myosin phosphatase target subunit, MYPT; and a smaller subunit, M20, of unknown function. Most of the properties of MP are due to MYPT and include binding of PP1c and substrate. Other interactions are discussed. A recent discovery is the existence of an MYPT family and members include, MYPT1, MYPT2, MBS85, MYPT3 and TIMAP. Characteristics of each are outlined. An important discovery was that the activity of MP could be regulated and both activation and inhibition were reported. Activation occurs in response to elevated cyclic nucleotide levels and various mechanisms are presented. Inhibition of MP is a major component of Ca2+-sensitization in smooth muscle and various molecular mechanisms are discussed. Two mechanisms are cited frequently: (1) Phosphorylation of an inhibitory site on MYPT1, Thr696 (human isoform) and resulting inhibition of PP1c activity. Several kinases can phosphorylate Thr696, including Rho-kinase that serves an important role in smooth muscle function; and (2) Inhibition of MP by the protein kinase C-potentiated inhibitor protein of 17 kDa (CPI-17). Examples where these mechanisms are implicated in smooth muscle function are presented. The critical role of RhoA/Rho-kinase signaling in various systems is discussed, in particular those vascular smooth muscle disorders involving hypercontractility.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:Molecular and Cellular Biochemistry. - 259 : 1-2 (2004), p. 197-209. -
További szerzők:Nakano, Takeshi Hartshorne, David J. Erdődi Ferenc (1953-) (biokémikus)
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12.

001-es BibID:BIBFORM075940
Első szerző:Kiss Andrea (biokémikus, vegyész)
Cím:Myosin phosphatase : unexpected functions of a long-known enzyme / Kiss Andrea, Erdődi Ferenc, Lontay Beáta
Dátum:2019
ISSN:0167-4889
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochimica et Biophysica Acta (BBA). Molecular Cell Research. - 1866 : 1 (2019), p. 2-15. -
További szerzők:Erdődi Ferenc (1953-) (biokémikus) Lontay Beáta (1975-) (biokémikus)
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EFOP-3.6.2-16-2017-00006
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